Coronavirus Spike Protein N-Glycosylation Site Detection

Glycoproteomic analyses of spike (S) proteins from two distinct gammacoronaviruses infecting marine mammals. The dataset catalogs over 100 N-glycans per trimer and identifies O-glycosylation sites, generated by researcher Ruben J. G. Hulswit and published via figshare in April 2026. It provides structural details on unique domains and glycosylation patterns.

Use Cases

• Analyze N-glycosylation site occupancy patterns across different spike protein domains like S1A, S1B, and the unique S1^0 domain.
• Correlate high-mannose glycan abundance on the S1^0 domain with potential immune evasion mechanisms.
• Map O-glycosylation sites within the described mucin-like loop at the trimer apex to study glycan shield density.
• Compare glycosylation profiles between the two gammacoronavirus spike proteins (75.7% sequence identity) to identify conserved modifications.
• Investigate the structural role of the unique ~200 residue N-terminal S1^0 domain, which has homology to the cupin protein superfamily.

Strengths

• Data derived from high-resolution cryo-EM structural studies of viral proteins.
• Glycoproteomic analysis identifies >100 N-glycans per spike protein trimer.
• Includes identification of O-glycosylation sites within specific protein loops.
• Directly associated with peer-reviewed structural biology research.

Limitations

• Dataset size is 22.9 KB, indicating a very limited number of records or observations.
• Specific row count and column names are not provided, limiting assessment of data volume and features.
• Focus is restricted to two specific gammacoronaviruses, limiting generalizability to other viral families.

Provenance

Source

Ruben J. G. Hulswit via figshare.

Collection Method

Cryo-electron microscopy and glycoproteomic analysis of purified viral spike proteins.

Freshness

Last updated April 2026.